| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1958041 | Biophysical Journal | 2007 | 7 Pages |
Abstract
Based on recent experimental evidences of the transmission of prion diseases due to a particular transmembrane form (termed CtmPrP), we propose a theoretical model for the molecular mechanism of such conformational diseases, in which a misfolded CtmPrP induces a similar misfolding of another CtmPrP. Computer simulations are performed to investigate the correlation between folding time and the concentration of misfolded PrP in various processes, including dimerization, trimerization, and cooperative dimerization. By comparing with the experimental correlation curve between incubation time and injected dose of scrapie prions, we conclude that cooperative dimerization may play an important role in the pathological mechanism of prion diseases.
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Authors
D.-M. Ou, C.-C. Chen, C.-M. Chen,